Origin of Energy Dissipation in the Oligomeric Fucoxanthin-Chlorophyll a/c Binding Proteins

Fucoxanthin-chlorophyll proteins (FCPs) are a family of photosynthetic light-harvesting complex (LHC) proteins found in diatoms. They efficiently capture photons and regulate their functions, ensuring diatom survival in highly fluctuating light. FCPs are present in different oligomeric states in vivo, but functional differences among these FCP oligomers are not yet fully understood. Here we characterized two types of antenna complexes (FCP-B/C dimers and FCP-A tetramers) that coexist in the marine centric diatom Chaetoceros gracilis using both time-resolved fluorescence and transient absorption spectroscopy. We found that the FCP-B/C complex did not show fluorescence quenching, whereas FCP-A was severely quenched, via an ultrafast excitation energy transfer (EET) pathway from Chl a Qy to the fucoxanthin S1/ICT state. These results highlight the functional differences between FCP dimers and tetramers and indicate that the EET pathway from Chl a to carotenoids is an energy dissipation mechanism conserved in a variety of photosynthetic organisms.